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      Asprosin, a Fasting-Induced Glucogenic Protein Hormone

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          SUMMARY

          Hepatic glucose release into the circulation is vital for brain function and survival during periods of fasting and is modulated by an array of hormones that precisely regulate plasma glucose levels. We have identified a fasting-induced protein hormone that modulates hepatic glucose release. It is the C-terminal cleavage product of profibrillin, and we name it Asprosin. Asprosin is secreted by white adipose, circulates at nanomolar levels, and is recruited to the liver, where it activates the G protein-cAMP-PKA pathway, resulting in rapid glucose release into the circulation. Humans and mice with insulin resistance show pathologically elevated plasma asprosin, and its loss of function via immunologic or genetic means has a profound glucose- and insulin-lowering effect secondary to reduced hepatic glucose release. Asprosin represents a glucogenic protein hormone, and therapeutically targeting it may be beneficial in type II diabetes and metabolic syndrome.

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          Journal
          0413066
          2830
          Cell
          Cell
          Cell
          0092-8674
          1097-4172
          7 March 2016
          14 April 2016
          21 April 2016
          21 April 2017
          : 165
          : 3
          : 566-579
          Affiliations
          [1 ]Department of Molecular and Cellular Biology, Baylor College of Medicine, Houston, TX 77030, USA
          [2 ]Department of Molecular and Human Genetics, Baylor College of Medicine, Houston, TX 77030, USA
          [3 ]Department of Pediatrics, Baylor College of Medicine, Houston, TX 77030, USA
          [4 ]Division of Cardiothoracic Surgery, Michael E. DeBakey Department of Surgery, Baylor College of Medicine, Houston, TX 77030, USA
          [5 ]Department of Internal Medicine, University of Texas Medical School at Houston, Houston, TX 77030, USA
          [6 ]Department of Pharmacology and Systems Therapeutics, Icahn School of Medicine at Mount Sinai, New York, NY 10029, USA
          Author notes
          [* ]Correspondence: chopra@ 123456bcm.edu
          Article
          PMC4852710 PMC4852710 4852710 nihpa765464
          10.1016/j.cell.2016.02.063
          4852710
          27087445
          cc576213-1738-476c-a127-241078476434
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